Job Results:

Ligand

Structure

Job ID

b66da62373d29d285a275497218b65f3

Job name

NA

Time

2024-11-27 22:32:54

Rank Target PDB ID AirScore Detail
41Intestinal maltase-glucoamylase (MGAM)3L4Y8.13
Target general information
Gen name
MGAM
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
MGAM
Protein family
Glycosyl hydrolase 31 family
Biochemical class
Glycosylase
Function
May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing.
Related diseases
Hypervalinemia and hyperleucine-isoleucinemia (HVLI) [MIM:618850]: An autosomal recessive metabolic disorder characterized by highly elevated plasma concentrations of valine and leucine/isoleucine. Affected individuals suffer from headache and mild memory impairment. {ECO:0000269|PubMed:25653144}. The disease is caused by variants affecting the gene represented in this entry. A patient with hypervalinemia and hyperleucine-isoleucinemia was identified as compound heterozygote for Gln-170 (inherited from his father) and Lys-264 (inherited from his mother), both variants reduced the catalytic activity of the enzyme. After treatment with vitamin B6, a precursor of pyridoxal 5'-phosphate, a BCAT2 cofactor, the blood levels of branched chain amino acids, especially valine, were decreased and brain lesions were improved. {ECO:0000269|PubMed:25653144}.
Drugs

(DrugBank ID)

DB00284; DB00491; DB04878
Interacts with
Q13520; Q7Z7G2; Q96BA8; O15529; P14410; P54219-3; Q9NUH8
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane; Multifunctional enzyme; Proteomics identification; Reference proteome; Repeat; Signal-anchor; Sulfation; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

97779.4
Length
863
Aromaticity
0.12
Instability index
32.47
Isoelectric point
5.2
Charge

(pH=7)

-28.27
2D Binding mode
Binding energy

(Kcal/mol)

-8.46
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
VNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWAH
Hydrogen bonds contact
Hydrophobic contact
42Beta-adrenergic receptor kinase 1 (ADRBK1)3V5W8.12
Target general information
Gen name
GRK2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
GRK2; G-protein coupled receptor kinase 2; BetaARK1; Beta-ARK-1; Beta ARK1
Protein family
Protein kinase superfamily, AGC Ser/Thr protein kinase family, GPRK subfamily
Biochemical class
Kinase
Function
Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner.
Related diseases
3-ketothiolase deficiency (3KTD) [MIM:203750]: An autosomal recessive inborn error of isoleucine catabolism characterized by intermittent ketoacidotic attacks associated with unconsciousness. Some patients die during an attack or are mentally retarded. Urinary excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, triglylglycine, butanone is increased. It seems likely that the severity of this disease correlates better with the environmental or acquired factors than with the ACAT1 genotype. {ECO:0000269|PubMed:1346617, ECO:0000269|PubMed:1715688, ECO:0000269|PubMed:7728148, ECO:0000269|PubMed:9744475}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00171
Interacts with
P05067; P48730-2; P21860; P21462; Q9Y2X7; P35626; Q00987; P13591; P25963; Q13635; P0CG48
EC number
EC 2.7.11.15
Uniprot keywords
3D-structure; ATP-binding; Cell membrane; Cell projection; Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Proteomics identification; Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

38433.9
Length
337
Aromaticity
0.09
Instability index
52.17
Isoelectric point
7.36
Charge

(pH=7)

1.05
2D Binding mode
Binding energy

(Kcal/mol)

-8.23
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
KNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEADMRFYAAEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGEVNAADAFDKGIKLLDSDQELYRNFPLTISERWQQEVAE
Hydrogen bonds contact
Hydrophobic contact
43Short transient receptor potential channel 5 (TRPC5)7WDB8.11
Target general information
Gen name
TRPC5
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
hTRP5; hTRP-5; TrpC5; Transient receptor protein 5; TRP-5
Protein family
Transient receptor (TC 1.A.4) family, STrpC subfamily, TRPC5 sub-subfamily
Biochemical class
Transient receptor potential catioin channel
Function
Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion.
Related diseases
Loss-of-function variants in TRPC5 may be involved in a mental disorder characterized by maladaptive behavior, anxiety, autism, postpartum depression, extreme food-seeking and hoarding behavior, hyperphagia and obesity. {ECO:0000269|PubMed:38959890}.
Drugs

(DrugBank ID)

NA
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport; Cell membrane; Disease variant; Glycoprotein; Ion channel; Ion transport; Membrane; Proteomics identification; Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

76850.6
Length
665
Aromaticity
0.12
Instability index
40.05
Isoelectric point
6.16
Charge

(pH=7)

-5.94
2D Binding mode
Binding energy

(Kcal/mol)

-8.87
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
RIPLQIVRAETELSAEEKAFLNAVEKGDYATVKQALQEAEIYYNVNINCMDPLGRSALLIAIENENLEIMELLLNHSVYVGDALLYAIRKEVVGAVELLLSYQFSEFTPDITPIMLAAHTNNYEIIKLLVQKRVTIPRPHQIRCNCVECVSSSEVDSLRHSRSRLNIYKALASPSLIALSSEDPILTAFRLGWELKELSKVENEFKAEYEELSQQCKLFAKDLLDQARSSRELEIILNHRDDLAKLKVAIKYHQKEFVAQPNCQQLLATLWYDGFPGWRRKHWVVKLLTCMTIGFLFPMLSIAYLISPRSNLGLFIKKPFIKFICHTASYLTFLFMLLLASQHVQGPPPTVVEWMILPWVLGFIWGEIKEMWDGGFTEYIHDWWNLMDFAMNSLYLATISLKIVAYVKYNGSRPREEWEMWHPTLIAEALFAISNILSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYETRAIDEPNNCKGIRCEKQNNAFSTLFETLQSLFWSVFGLLNLYVTNVKARHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFDEGGTLPPPFNIISLIQNQHYQEVIRNLVKRYVAAMIRNSKTTEENFKELKQDISSFRYEVLDLL
Hydrogen bonds contact
Hydrophobic contact
44Cannabinoid receptor 2 (CB2)6PT08.11
Target general information
Gen name
CNR2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
hCB2; Cannabinoid CB2 receptor; CX5; CB2B; CB2A; CB-2
Protein family
G-protein coupled receptor 1 family
Biochemical class
GPCR rhodopsin
Function
May function in inflammatory response, nociceptive transmission and bone homeostasis. Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase.
Related diseases
Factor V deficiency (FA5D) [MIM:227400]: A blood coagulation disorder leading to a hemorrhagic diathesis known as parahemophilia. {ECO:0000269|PubMed:10942390, ECO:0000269|PubMed:12393490}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Thrombophilia due to activated protein C resistance (THPH2) [MIM:188055]: A hemostatic disorder due to defective degradation of factor V by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis. {ECO:0000269|PubMed:10391209, ECO:0000269|PubMed:10942390, ECO:0000269|PubMed:11435304, ECO:0000269|PubMed:11858490, ECO:0000269|PubMed:14617013, ECO:0000269|PubMed:14695241, ECO:0000269|PubMed:16710414, ECO:0000269|PubMed:8164741, ECO:0000269|PubMed:9454742}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. {ECO:0000269|PubMed:9245936}. Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:15534175}. Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Pregnancy loss, recurrent, 1 (RPRGL1) [MIM:614389]: A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions. {ECO:0000269|PubMed:11018168}. Disease susceptibility is associated with variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB09061; DB00470; DB06202; DB14009; DB00486; DB14011; DB02955; DB16321; DB11755
Interacts with
Q9UKJ8; Q15848; Q9NRZ5; P13236; P21964; Q14802-3; Q8N387; Q8IXM6; I3L0A0; Q96AA3; Q9Y6D0; Q6ICL7; Q9NP94; Q13501; Q96HH6; Q969S6; Q9NWH2; Q9H2L4; Q8N2M4; Q6ZT21; Q5TGU0; Q9Y548; Q9BSR8; Q96EC8
EC number
NA
Uniprot keywords
3D-structure; Cell membrane; Cell projection; G-protein coupled receptor; Glycoprotein; Inflammatory response; Membrane; Phosphoprotein; Proteomics identification; Receptor; Reference proteome; Transducer; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
R
Molecular weight

(Da)

32999.2
Length
298
Aromaticity
0.11
Instability index
30.98
Isoelectric point
9.49
Charge

(pH=7)

14.35
2D Binding mode
Binding energy

(Kcal/mol)

-9.12
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
MKDYMILSGPQKTAVAVLCTLLGLLSALENVAVLYLILSSHQLRRKPSYLFIGSLAGADFLASVVFACSFVNFHVFHGVDSKAVFLLKIGSVTMTFTASVGSLLLTAIDRYLCLRYPPSYKALLTRGRALVTLGIMWVLSALVSYLPLMGWTCCPRPCSELFPLIPNDYLLSWLLFIAFLFSGIIYTYGHVLWKAHQHVASLSGHQDRQVPGMARMRLDVRLAKTLGLVLAVLLICWFPVLALMAHSLATTLSDQVKKAFAFCSMLCLINSMVNPVIYALRSGEIRSSAHHCLAHWKK
Hydrogen bonds contact
Hydrophobic contact
45Pol polyprotein5KAO8.10
Target general information
Gen name
pol
Organism
Human immunodeficiency virus type 1 (HIV-1)
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
NA
Biochemical class
Hydrolase / hydrolase inhibitor
Function
Aspartic-type endopeptidase activity.
Related diseases
Oocyte/zygote/embryo maturation arrest 16 (OZEMA16) [MIM:617234]: A rare cause of female primary infertility. In affected women, ovulation and fertilization proceed normally but embryos are arrested at early stages of development. Inheritance is autosomal recessive. {ECO:0000269|PubMed:27545678}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00701; DB01072; DB04887; DB01264; DB01319; DB00224; DB01601; DB00503; DB01232; DB00932
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Aspartyl protease; Hydrolase; Protease
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

21411
Length
198
Aromaticity
0.05
Instability index
42.78
Isoelectric point
9.45
Charge

(pH=7)

4.15
2D Binding mode
Binding energy

(Kcal/mol)

-8.55
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
PQVTLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGATLNFPQVTLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGATLNF
Hydrogen bonds contact
Hydrophobic contact
46Phosphodiesterase 3A (PDE3A)7EG08.10
Target general information
Gen name
PDE3A
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
cGMP-inhibited 3',5'-cyclic phosphodiesterase A; Phosphodiesterase 3A; Cyclic GMP-inhibited phosphodiesterase A; Cyclic GMP inhibited phosphodiesterase A; CGI-PDE A
Protein family
Cyclic nucleotide phosphodiesterase family, PDE3 subfamily
Biochemical class
Phosphoric diester hydrolase
Function
Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes.
Related diseases
Hypertension and brachydactyly syndrome (HTNB) [MIM:112410]: A syndrome characterized by brachydactyly type E, severe salt-independent but age-dependent hypertension, an increased fibroblast growth rate, neurovascular contact at the rostral-ventrolateral medulla, and altered baroreflex blood pressure regulation. It results in death from stroke before age 50 years when untreated. Brachydactyly type E is characterized by shortening of the fingers mainly in the metacarpals and metatarsals. {ECO:0000269|PubMed:25961942}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB01223; DB01427; DB00261; DB00201; DB01166; DB04880; DB05266; DB00922; DB00235; DB01303; DB00277; DB08811; DB09283
Interacts with
Q9Y6D6; Q9Y6D5
EC number
EC 3.1.4.17
Uniprot keywords
3D-structure; cAMP; cGMP; Cytoplasm; Direct protein sequencing; Disease variant; Hydrolase; Isopeptide bond; Manganese; Membrane; Metal-binding; Phosphoprotein; Proteomics identification; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

108171
Length
939
Aromaticity
0.11
Instability index
39.75
Isoelectric point
6.53
Charge

(pH=7)

-4.15
2D Binding mode
Binding energy

(Kcal/mol)

-9.29
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
KPILAPEPLVMDNLDSIMEQLNTWNFPIFDLVENIGRKCGRILSQVSYRLFEDMGLFEAFKIPIREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLSTVGYVFSKTYNVTDDKYGCLSGNIPALELMALYVAAAMHDYDHPGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLINLDHVEFKHFRFLVIEAILATDLKKHFDFVAKFNGKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKELHLQWTDGIVNEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCNSYDSAGLMPGKWVEKIYCQITQHLLQNHKMWKKVIEEEQRLAGIENQNISVDLETNYAELVLDVGRVTLGENSRKKMKDCKLRKKQNESVSRAMCALLNSGGGVIKAEIENEDYSYTKDGIGLDLENSFSNILLFVPEYLDFMQNGNYFLIFVKSWSLNTSGLRITTLSSNLYKRDITSAKVMNATAALEFLKDMKKTRGRLYLRPELLAKRPCVDIQEENNMKALAGVFFDRTELDRKEKLTFTESTHVEIKNFSTERLLQRIKEILPQYVSAFANTDGGYLFIGLNEDKEIIGFKAEMSDLDDLEREIEKSIRKMPVHHFCMEKKKINYSCKFLGVYDKGSLCGYVCALRVERFCCAVFAKEPDSWHVKDNRVMQLTRKEWIQFMVEAEPKFSSAYEEVISQINTSLPAPHSWPLLEWQRQRHHCPGLSGRITYTPENLCRKLFLQHEGLKQLICEEMSSVRKGSLIFSRSWSVDLGLQENHKVLCDALLISQDSPPVLYTFHMVQDEEFKGYSTQTALTLKQKLAKIGGYTKKVCVMTKIFYLSPEGMTSCQYDLRSQVIYPESYYFTRRKYLLKALFKALKRLKSLRDQFSFAENLYQIIGIDCFQKNDK
Hydrogen bonds contact
Hydrophobic contact
47Metabotropic glutamate receptor 3 (mGluR3)4XAR8.10
Target general information
Gen name
GRM3
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
mGLUR3; Group III metabotropic glutamate receptor; GPRC1C
Protein family
G-protein coupled receptor 3 family
Biochemical class
GPCR glutamate
Function
Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. G-protein coupled receptor for glutamate.
Related diseases
Paramyotonia congenita (PMC) [MIM:168300]: An autosomal dominant channelopathy characterized by myotonia, increased by exposure to cold, intermittent flaccid paresis, not necessarily dependent on cold or myotonia, lability of serum potassium, non-progressive nature and lack of atrophy or hypertrophy of muscles. In some patients, myotonia is not increased by cold exposure (paramyotonia without cold paralysis). Patients may have a combination phenotype of PMC and HYPP. {ECO:0000269|PubMed:10369308, ECO:0000269|PubMed:10727489, ECO:0000269|PubMed:1310898, ECO:0000269|PubMed:1316765, ECO:0000269|PubMed:1338909, ECO:0000269|PubMed:15318338, ECO:0000269|PubMed:15790667, ECO:0000269|PubMed:16786525, ECO:0000269|PubMed:18166706, ECO:0000269|PubMed:18690054, ECO:0000269|PubMed:19077043, ECO:0000269|PubMed:20076800, ECO:0000269|PubMed:8242056, ECO:0000269|PubMed:8308722, ECO:0000269|PubMed:8388676, ECO:0000269|PubMed:8580427}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Periodic paralysis hypokalemic 2 (HOKPP2) [MIM:613345]: An autosomal dominant disorder manifested by episodic flaccid generalized muscle weakness associated with falls of serum potassium levels. {ECO:0000269|PubMed:10599760, ECO:0000269|PubMed:10851391, ECO:0000269|PubMed:10944223, ECO:0000269|PubMed:11558801, ECO:0000269|PubMed:11591859, ECO:0000269|PubMed:16890191, ECO:0000269|PubMed:17898326, ECO:0000269|PubMed:18162704, ECO:0000269|PubMed:19118277, ECO:0000269|PubMed:20522878, ECO:0000269|PubMed:21043388, ECO:0000269|PubMed:24549961}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Periodic paralysis hyperkalemic (HYPP) [MIM:170500]: An autosomal dominant channelopathy characterized by episodic flaccid generalized muscle weakness associated with high levels of serum potassium. Concurrence of myotonia is found in HYPP patients. {ECO:0000269|PubMed:1659668, ECO:0000269|PubMed:1659948, ECO:0000269|PubMed:20076800}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Periodic paralysis normokalemic (NKPP) [MIM:170500]: A disorder closely related to hyperkalemic periodic paralysis, but marked by a lack of alterations in potassium levels during attacks of muscle weakness. {ECO:0000269|PubMed:15596759, ECO:0000269|PubMed:18046642, ECO:0000269|PubMed:20522878}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Myotonia SCN4A-related (MYOSCN4A) [MIM:608390]: A phenotypically highly variable myotonia aggravated by potassium loading, and sometimes by cold. Myotonia is characterized by sustained muscle tensing that prevents muscles from relaxing normally. It causes muscle stiffness that can interfere with movement. In some people the stiffness is very mild, while in other cases it may be severe enough to interfere with walking, running, and other activities of daily life. Myotonia SCN4A-related includes myotonia permanens and myotonia fluctuans. In myotonia permanens, the myotonia is generalized and there is a hypertrophy of the muscle, particularly in the neck and the shoulder. Attacks of severe muscle stiffness of the thoracic muscles may be life threatening due to impaired ventilation. In myotonia fluctuans, the muscle stiffness may fluctuate from day to day, provoked by exercise. {ECO:0000269|PubMed:10218481, ECO:0000269|PubMed:16786525, ECO:0000269|PubMed:16832098, ECO:0000269|PubMed:17212350, ECO:0000269|PubMed:17998485, ECO:0000269|PubMed:18203179, ECO:0000269|PubMed:18337100, ECO:0000269|PubMed:19015483, ECO:0000269|PubMed:19347921, ECO:0000269|PubMed:20076800, ECO:0000269|PubMed:27653901, ECO:0000269|PubMed:8058156, ECO:0000269|PubMed:9392583}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 16 (CMS16) [MIM:614198]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS16 is characterized by fatigable generalized weakness and recurrent attacks of respiratory and bulbar paralysis since birth. The fatigable weakness involves lid-elevator, external ocular, facial, limb and truncal muscles and an decremental response of the compound muscle action potential on repetitive stimulation. {ECO:0000269|PubMed:12766226, ECO:0000269|PubMed:25707578, ECO:0000269|PubMed:26659129}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Congenital myopathy 22A, classic (CMYO22A) [MIM:620351]: A form of congenital myopathy, a clinically and genetically heterogeneous group of muscle disorders characterized by hypotonia and muscle weakness apparent at birth, and specific pathological features on muscle biopsy. CMYO22A is an autosomal recessive form characterized by fetal hypokinesia, polyhydramnios, and severe neonatal hypotonia associated with respiratory insufficiency. Affected individuals who survive the neonatal period have delayed motor development, difficulty walking, proximal muscle weakness of the upper and lower limbs, facial and neck muscle weakness, easy fatigability, and mild limb contractures or foot deformities. {ECO:0000269|PubMed:26700687, ECO:0000269|PubMed:28262468, ECO:0000269|PubMed:36090556}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Congenital myopathy 22B, severe fetal (CMYO22B) [MIM:620369]: A severe congenital myopathy, a clinically and genetically heterogeneous group of muscle disorders characterized by hypotonia and muscle weakness apparent at birth, and specific pathological features on muscle biopsy. CMYO22B is an autosomal recessive form characterized by onset in utero. Affected individuals show fetal akinesia, and develop fetal hydrops with pulmonary hypoplasia, severe joint contractures, and generalized muscle hypoplasia. Death occurs in utero or soon after birth. {ECO:0000269|PubMed:26700687}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB05096
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; Proteomics identification; Receptor; Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

50355.5
Length
445
Aromaticity
0.11
Instability index
38.26
Isoelectric point
6.52
Charge

(pH=7)

-1.53
2D Binding mode
Binding energy

(Kcal/mol)

-8.93
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
RREIKIEGDLVLGGLFPINEKGTGTEECGRINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNISIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRANASFTWVASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFRDFWEQKFQCSLRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKLCDAMKILDGKKLYKDYLLKINFTAPDADSIVKFDTFGDGMGRYNVFNFQNVGGKYSYLKVGHWAETLSLDVNSIHWSRNSVPTSE
Hydrogen bonds contact
Hydrophobic contact
48Steroid 21-hydroxylase4Y8W8.10
Target general information
Gen name
CYP21A2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
CYP21;CYP21B
Protein family
Cytochrome P450 family
Biochemical class
Oxidoreductase
Function
Heme binding.Iron ion binding.Steroid 21-monooxygenase activity.Steroid binding.Steroid hydroxylase activity.
Related diseases
Adrenal hyperplasia 3 (AH3) [MIM:201910]: A form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late-onset (NC or LOAH) and 'cryptic' (asymptomatic). {ECO:0000269|PubMed:10051010, ECO:0000269|PubMed:10094562, ECO:0000269|PubMed:10198222, ECO:0000269|PubMed:10364682, ECO:0000269|PubMed:10391209, ECO:0000269|PubMed:10408778, ECO:0000269|PubMed:10408786, ECO:0000269|PubMed:10443693, ECO:0000269|PubMed:10496074, ECO:0000269|PubMed:10720040, ECO:0000269|PubMed:11232002, ECO:0000269|PubMed:11598371, ECO:0000269|PubMed:11600539, ECO:0000269|PubMed:11746135, ECO:0000269|PubMed:12213891, ECO:0000269|PubMed:12222711, ECO:0000269|PubMed:12788866, ECO:0000269|PubMed:12887291, ECO:0000269|PubMed:12915679, ECO:0000269|PubMed:1406699, ECO:0000269|PubMed:1406709, ECO:0000269|PubMed:14676460, ECO:0000269|PubMed:14715874, ECO:0000269|PubMed:1496017, ECO:0000269|PubMed:15110320, ECO:0000269|PubMed:15126570, ECO:0000269|PubMed:16046588, ECO:0000269|PubMed:1644925, ECO:0000269|PubMed:16984992, ECO:0000269|PubMed:18319307, ECO:0000269|PubMed:18381579, ECO:0000269|PubMed:18445671, ECO:0000269|PubMed:1864962, ECO:0000269|PubMed:1937474, ECO:0000269|PubMed:20080860, ECO:0000269|PubMed:2072928, ECO:0000269|PubMed:21169732, ECO:0000269|PubMed:22014889, ECO:0000269|PubMed:2303461, ECO:0000269|PubMed:27721825, ECO:0000269|PubMed:29328376, ECO:0000269|PubMed:3038528, ECO:0000269|PubMed:3257825, ECO:0000269|PubMed:3260007, ECO:0000269|PubMed:3267225, ECO:0000269|PubMed:3497399, ECO:0000269|PubMed:3871526, ECO:0000269|PubMed:7749410, ECO:0000269|PubMed:8478006, ECO:0000269|PubMed:8485582, ECO:0000269|PubMed:8989258, ECO:0000269|PubMed:9067760, ECO:0000269|PubMed:9187661, ECO:0000269|PubMed:9497336}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB01026; DB05667
Interacts with
NA
EC number
1.14.14.16
Uniprot keywords
3D-structure; Alternative splicing; Congenital adrenal hyperplasia; Disease variant; Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Lipid-binding; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Proteomics identification; Reference proteome; Steroid-binding; Steroidogenesis
Protein physicochemical properties
Chain ID
A,B,C
Molecular weight

(Da)

50326.2
Length
442
Aromaticity
0.08
Instability index
50.06
Isoelectric point
7.79
Charge

(pH=7)

2.07
2D Binding mode
Binding energy

(Kcal/mol)

-8.95
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
KLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIYRLHLGLQDVVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSRNYPDLSLGDYSLLWKAHKKLTRSALLLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTFGDKIKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLKQAIEKRDHIVEMQLRQHKESLVAGQWRDMMDYMLQGVAGQLLEGHVHMAAVDLLIGGTETTANTLSWAVVFLLHHPEIQQRLQEELDHESRVPYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRPSSISGYDIPEGTVIIPNLQGAHLDETVWERPHEFWPDRFLEPGKNSRALAFGCGARVCLGEPLARLELFVVLTRLLQAFTLLPSGDALPSLQPLPHCSVILKMQPFQVRLQPRG
Hydrogen bonds contact
Hydrophobic contact
49Ephrin type-A receptor 7 (EPHA7)3DKO8.09
Target general information
Gen name
EPHA7
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
hEK11; EPH-like kinase 11; EPH homology kinase 3; EK11; EHK3; EHK-3
Protein family
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
Biochemical class
Kinase
Function
The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 AND MAPK3 which are phosphorylated upon activation of EPHA7. Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells.
Related diseases
WHIM syndrome 2 (WHIMS2) [MIM:619407]: An autosomal recessive form of WHIM syndrome, a primary immunodeficiency disorder characterized by warts, hypogammaglobulinemia, infections, and myelokathexis. Myelokathexis is a unique form of non-cyclic severe congenital neutropenia caused by accumulation of mature and degenerating neutrophils in the bone marrow. Monocytopenia and lymphopenia, especially B lymphopenia, also commonly occur. There is significant phenotypic variation among patients, such that some individuals may have an incomplete form of the disorder in which one or more of the classic tetrad features are not present. {ECO:0000269|PubMed:24777453}. The disease may be caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07970; DB12010
Interacts with
P07333; P52803; P29317; P29320; P29323; P54760; Q16288; P52793
EC number
EC 2.7.10.1
Uniprot keywords
3D-structure; Alternative splicing; Apoptosis; ATP-binding; Cell membrane; Developmental protein; Glycoprotein; Kinase; Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein; Proteomics identification; Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

31250.7
Length
275
Aromaticity
0.09
Instability index
28.85
Isoelectric point
6.44
Charge

(pH=7)

-1.92
2D Binding mode
Binding energy

(Kcal/mol)

-9.17
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
TYIDPETYEDPNRAVHQFAKELDASCIKIERVIGAEFGEVCSGRLKLPGKRDVAVAIKTLKVGYTEKQRRDFLCEASIMGQFDHPNVVHLEGVVTRGKPVMIVIEFMENGALDAFLRKHDGQFTVIQLVGMLRGIAAGMRYLADMGYVHRDLAARNILVNSNLVCKVSDFGPVRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPAPMDCPAGLHQLMLDCWQKERAERPKFEQIVGILDKMIRNPNSAHH
Hydrogen bonds contact
Hydrophobic contact
50Extracellular lysophospholipase D (E-NPP2)4ZGA8.09
Target general information
Gen name
ENPP2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
LysoPLD; Ectonucleotide pyrophosphatase/phosphodiesterase family member 2; E-NPP 2; Autotaxin; ATX
Protein family
Nucleotide pyrophosphatase/phosphodiesterase family
Biochemical class
Phosphoric diester hydrolase
Function
Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development (Probable). Tumor cell motility-stimulating factor.
Related diseases
Anemia, non-spherocytic hemolytic, due to G6PD deficiency (NSHA) [MIM:300908]: A disease characterized by G6PD deficiency, acute hemolytic anemia, fatigue, back pain, and jaundice. In most patients, the disease is triggered by an exogenous agent, such as some drugs, food, or infection. Increased unconjugated bilirubin, lactate dehydrogenase, and reticulocytosis are markers of the disorder. Although G6PD deficiency can be life-threatening, most patients are asymptomatic throughout their life. {ECO:0000269|PubMed:12524354, ECO:0000269|PubMed:1303180, ECO:0000269|PubMed:1303182, ECO:0000269|PubMed:1536798, ECO:0000269|PubMed:1611091, ECO:0000269|PubMed:1889820, ECO:0000269|PubMed:1945893, ECO:0000269|PubMed:20007901, ECO:0000269|PubMed:26479991, ECO:0000269|PubMed:2836867, ECO:0000269|PubMed:2912069, ECO:0000269|PubMed:30988594, ECO:0000269|PubMed:38066190, ECO:0000269|PubMed:7858267, ECO:0000269|PubMed:7959695, ECO:0000269|PubMed:8193373, ECO:0000269|PubMed:8490627, ECO:0000269|PubMed:8533762, ECO:0000269|PubMed:8733135, ECO:0000269|PubMed:9452072}. The disease is caused by variants affecting the gene represented in this entry. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of NSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.
Drugs

(DrugBank ID)

NA
Interacts with
NA
EC number
EC 3.1.4.39
Uniprot keywords
3D-structure; Alternative splicing; Calcium; Chemotaxis; Cleavage on pair of basic residues; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Obesity; Proteomics identification; Reference proteome; Repeat; Secreted; Signal; Zinc
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

85397.4
Length
740
Aromaticity
0.12
Instability index
58.63
Isoelectric point
7.16
Charge

(pH=7)

1.02
2D Binding mode
Binding energy

(Kcal/mol)

-8.6
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
GSCKGRCFELCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGNEENACHCEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFDPKAIIANLTCKKPDQHFKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPFFQGDHGFDNKVNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTMPEEVTRPNYPGIMYLQSDFDLGTEERHLLYGRPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQACVRPDVRVSPSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFRKTSRSYPEILTLKTYLHTYE
Hydrogen bonds contact
Hydrophobic contact
51Transferrin (TF)1RYO8.09
Target general information
Gen name
TF
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Siderophilin; Serotransferrin; PRO1400; Beta-1 metal-binding globulin
Protein family
Transferrin family
Biochemical class
Transferrin
Function
It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.
Related diseases
Atransferrinemia (ATRAF) [MIM:209300]: A rare autosomal recessive disorder characterized by abnormal synthesis of transferrin leading to iron overload and microcytic hypochromic anemia. {ECO:0000269|PubMed:11110675, ECO:0000269|PubMed:15466165}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB01370; DB14517; DB14518; DB01294; DB14526; DB14527; DB11136; DB14528; DB14529; DB14530; DB00515; DB09130; DB11397; DB13949; DB14490; DB14491; DB14488; DB14501; DB14489; DB13257; DB06215; DB06784; DB05260; DB01592; DB00893; DB00677; DB06757; DB11182; DB14520; DB01593; DB14487; DB14533; DB14548
Interacts with
O43315; O00501; Q7Z7G2; Q9GZR5; Q9Y282; Q96KR6; P01350; P08034; Q8NBJ4; O15529; Q8TED1; Q7Z5P4; A8MZ59; O15173; Q96TC7; Q3KNW5; Q9BXS9-3; Q99523; O43278-2; Q8N9I0; P02786; Q4KMG9; Q9K0U9; Q09057; Q9K0V0; P02786
EC number
NA
Uniprot keywords
3D-structure; Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport; Metal-binding; Methylation; Phosphoprotein; Proteomics identification; Reference proteome; Repeat; Secreted; Signal; Transport
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

35854.5
Length
324
Aromaticity
0.1
Instability index
34.17
Isoelectric point
7.58
Charge

(pH=7)

1.42
2D Binding mode
Binding energy

(Kcal/mol)

-8.99
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
KTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLR
Hydrogen bonds contact
Hydrophobic contact
52Zinc finger protein Helios (IKZF2)7LPS8.08
Target general information
Gen name
IKZF2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Ikaros family zinc finger protein 2
Protein family
Ikaros C2H2-type zinc-finger protein family
Biochemical class
NA
Function
Associates with Ikaros at centromeric heterochromatin.
Related diseases
Developmental and epileptic encephalopathy 25, with amelogenesis imperfecta (DEE25) [MIM:615905]: An autosomal recessive disease characterized by subclinical seizures appearing in the first days of life, evolving to severe epileptic disease. Affected individuals have profound or severe delayed development with lack of speech, and most patients do not acquire the ability to sit. Additional variable features include axial hypotonia, peripheral hypertonia, and abnormal involuntary movements such as dystonia and choreoathetosis. Dental abnormalities, including delayed eruption, hypodontia, tooth hypoplasia, yellow discoloration, thin enamel, and enamel chipping are observed in most patients. {ECO:0000269|PubMed:24995870, ECO:0000269|PubMed:26384929, ECO:0000269|PubMed:30054523}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
P29972; P56545; P56545-3; Q17RB8; P09022; Q8N8B7-2
EC number
NA
Uniprot keywords
3D-structure; Acetylation; Activator; Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger
Protein physicochemical properties
Chain ID
B,C
Molecular weight

(Da)

47006.6
Length
410
Aromaticity
0.09
Instability index
44.28
Isoelectric point
7.23
Charge

(pH=7)

0.69
2D Binding mode
Binding energy

(Kcal/mol)

-8.99
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
INFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDGERPFHCNQCGASFTQKGNLLRHIKLHSG
Hydrogen bonds contact
Hydrophobic contact
53Choline O-acetyltransferase2FY38.07
Target general information
Gen name
CHAT
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
Carnitine/choline acetyltransferase family
Biochemical class
Transferase
Function
Choline O-acetyltransferase activity.
Related diseases
Myasthenic syndrome, congenital, 6, presynaptic (CMS6) [MIM:254210]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS6 affected individuals have myasthenic symptoms since birth or early infancy, negative tests for anti-AChR antibodies, and abrupt episodic crises with increased weakness, bulbar paralysis, and apnea precipitated by undue exertion, fever, or excitement. CMS6 inheritance is autosomal recessive. {ECO:0000269|PubMed:11172068, ECO:0000269|PubMed:12756141}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00122; DB14006; DB00184
Interacts with
Q6H8Q1-8; Q8N302-2; Q9NXL2-1; Q6XD76; Q9UII2; Q8TBE0; Q9UQB8-6; Q9ULD4-2; Q9NSI6-4; Q6P5X5; Q96LL4; P20807-4; O00257-3; Q6ZP82-1; O95674; Q9H3R5; Q8WUX9; Q9H2A9; Q3SX64; Q92782-2; Q14117; O14641; Q658K8; Q6UXG2-3; O00472; Q6NXG1; Q15910-2; Q8IZU1; P15407; P55318; Q06547-3; P23769-2; P23771; Q15486; Q8IV36; Q4VB01; Q53GQ0; P10809; P41134; Q9NZH6; Q8NA54; Q86U28; P17275; Q8N5Z5; Q6P597; P08727; Q14525; Q8IUC2; Q6IAA8; Q14847-2; P27338; Q9GZQ8; Q53S70; Q5JXC2; A0A0A0MR05; Q8NEH6; Q8TCY5; Q6IN84-2; Q96H12; P01106; P41271-2; P14598; Q9GZM8; Q5BJF6-2; Q9H8K7; Q9NR21-5; Q5VU43-8; Q13956; Q5SXH7-1; Q96T60; Q96I34; Q86UA1; Q15311; Q8TBY0; Q04206; P47804-3; Q9H0X6; P62899; Q66K80; Q9BY12-3; Q86SQ7-2; Q7Z6I5; Q496A3; Q7Z698; Q9C004; Q92783-2; Q8N4C7; O75528; Q15814; O15273; Q96A09; Q8WTV1; Q53NU3; Q71RG4-4; Q86WT6-2; Q9Y3Q8; Q99598; P49459; P11441; Q9H270; P19544-6; Q53FD0-2; Q3KNS6-3
EC number
2.3.1.6
Uniprot keywords
3D-structure; Acyltransferase; Alternative splicing; Congenital myasthenic syndrome; Direct protein sequencing; Disease variant; Neurotransmitter biosynthesis; Phosphoprotein; Proteomics identification; Reference proteome; Transferase
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

66365.9
Length
595
Aromaticity
0.08
Instability index
53.36
Isoelectric point
8.16
Charge

(pH=7)

4.64
2D Binding mode
Binding energy

(Kcal/mol)

-9.11
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
SEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQQKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNAAARLPPIGLLTSDGRSEWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHMTQPELVRSPMVPLPAPRRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQLAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLLKDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCAALPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCAATSSSKFAKAVEESLIDMRDLCSLLPP
Hydrogen bonds contact
Hydrophobic contact
54Prostaglandin D2 receptor 2 (PTGDR2)6D268.06
Target general information
Gen name
PTGDR2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
PTGDR2; Chemoattractant receptor-homologous molecule expressed on Th2 cells; CD294
Protein family
G-protein coupled receptor 1 family
Biochemical class
GPCR rhodopsin
Function
Receptor for prostaglandin D2 (PGD2). Coupled to the G(i)-protein. Receptor activation may result in pertussis toxin- sensitive decreases in cAMP levels and Ca(2+) mobilization. PI3K signaling is also implicated in mediating PTGDR2 effects. PGD2 induced receptor internalization. CRTH2 internalization can be regulated by diverse kinases such as, PKC, PKA, ADRBK1/GRK2, GPRK5/GRK5 and GRK6. Receptoractivation is responsible, at least in part, in immune regulation and allergic/inflammation responses.
Related diseases
Neurodevelopmental disorder with seizures, hypotonia, and brain imaging abnormalities (NEDSHBA) [MIM:618922]: An autosomal recessive neurodevelopmental disorder characterized by global developmental delay, hypotonia, severe to profound intellectual disability, early-onset epilepsy, and microcephaly. Neuroimaging shows cerebral atrophy, thin corpus callosum and hypomyelination in a majority of cases. Death in childhood may occur. {ECO:0000269|PubMed:27435318, ECO:0000269|PubMed:28097321, ECO:0000269|PubMed:32286009, ECO:0000269|PubMed:33476302, ECO:0000269|PubMed:33500274}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00770; DB12789; DB00917; DB01088; DB00328; DB02056; DB13036; DB00605; DB04828
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; Proteomics identification; Receptor; Reference proteome; Transducer; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

49740.6
Length
447
Aromaticity
0.1
Instability index
37.89
Isoelectric point
10.13
Charge

(pH=7)

21.88
2D Binding mode
Binding energy

(Kcal/mol)

-8.84
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
ATLKPLCPILEQMSRLQSHSATSIRYIDHAAVLLHGLASLLGLVENGVILFVVGCRMRQTVVTTWVLHLALSDLLASASLPFFTYFLAVGHSWELGTTFCKLHSSIFFLNMFASGFLLSAISLDRCLQVVRPVWAQNHRTVAAAHKVCLVLWALAVLNTVPYFVFRDTISRLDGRIMCYYNVLLLNPGPDRDATCNSRQAALAVSKFLLAFLVPLAIIASSHAAVSLRLQHRADLGLQHRNIFEMLRIDEGGGSGGDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYRRRPGRFVRLVAAVVAAFALCWGPYHVFSLLEARAHANPGLRPLVWRGLPFVTSLAFFNSVANPVLYVLTXPDMLRKLRRSLRTVLESVL
Hydrogen bonds contact
Hydrophobic contact
55Oxygen-insensitive NADPH nitroreductase3QDL8.06
Target general information
Gen name
rdxA
Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Uniprot ID
TTD ID
NA
Synonyms
HP_0954
Protein family
Nitroreductase family
Biochemical class
Oxidoreductase
Function
Oxidoreductase activity.
Related diseases
Hypervalinemia and hyperleucine-isoleucinemia (HVLI) [MIM:618850]: An autosomal recessive metabolic disorder characterized by highly elevated plasma concentrations of valine and leucine/isoleucine. Affected individuals suffer from headache and mild memory impairment. {ECO:0000269|PubMed:25653144}. The disease is caused by variants affecting the gene represented in this entry. A patient with hypervalinemia and hyperleucine-isoleucinemia was identified as compound heterozygote for Gln-170 (inherited from his father) and Lys-264 (inherited from his mother), both variants reduced the catalytic activity of the enzyme. After treatment with vitamin B6, a precursor of pyridoxal 5'-phosphate, a BCAT2 cofactor, the blood levels of branched chain amino acids, especially valine, were decreased and brain lesions were improved. {ECO:0000269|PubMed:25653144}.
Drugs

(DrugBank ID)

DB00916
Interacts with
NA
EC number
1.-.-.-
Uniprot keywords
3D-structure; Antibiotic resistance; NADP; Oxidoreductase; Reference proteome
Protein physicochemical properties
Chain ID
A,B,C,D
Molecular weight

(Da)

40094.3
Length
352
Aromaticity
0.08
Instability index
55.15
Isoelectric point
6.72
Charge

(pH=7)

-0.86
2D Binding mode
Binding energy

(Kcal/mol)

-8.37
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
MQRLESYILMKFLDQEKRRQLLNERHSCKMFDSHYEFSSTELEEIAEIARLSPSSYNTQPWHFVMVTDKDLKKQIAAHSYFNEEMIKSASALMVVCSLSYILEQCYIAVGQICMGVSLMGLDSCIIGGFDPLKVGEVLEERINPKIACLIALGKRVAEASQKSRKSKVDAITWLMKFLDQEKRRQLLNERHSCKMFDSHYEFSSTELEEIAEIARLSPSSYNTQPWHFVMVTDKDLKKQIAAHSYFNEEMIKSASALMVVCSLRPSELLPMQRLESYILEQCYIAVGQICMGVSLMGLDSCIIGGFDPLKVGEVLEERINKPKIACLIALGKRVAEASQKSRKSKVDAITWL
Hydrogen bonds contact
Hydrophobic contact
56Angiopoietin 1 receptor (TEK)3BEA8.06
Target general information
Gen name
TEK
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
hTIE2; VMCM1; VMCM; Tyrosine-protein kinase receptor TIE-2; Tyrosine-protein kinase receptor TEK; Tyrosine kinase with Ig and EGF homology domains-2; Tunica interna endothelial cell kinase; TIE2; P140
Protein family
Protein kinase superfamily, Tyr protein kinase family, Tie subfamily
Biochemical class
Kinase
Function
Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1. Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence.
Related diseases
Dominantly inherited venous malformations (VMCM) [MIM:600195]: An error of vascular morphogenesis characterized by dilated, serpiginous channels. {ECO:0000269|PubMed:10369874, ECO:0000269|PubMed:19079259, ECO:0000269|PubMed:19888299, ECO:0000269|PubMed:8980225}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Somatic mutations of TEK are associated with solitary and multiple sporadic venous malformations. {ECO:0000269|PubMed:19079259}.; DISEASE: May play a role in a range of diseases with a vascular component, including neovascularization of tumors, psoriasis and inflammation.; DISEASE: Glaucoma 3, primary congenital, E (GLC3E) [MIM:617272]: An autosomal dominant form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor. {ECO:0000269|PubMed:27270174}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00415; DB12010; DB08221; DB08901; DB08896; DB14840; DB11800; DB05294
Interacts with
Q15389; O15123; O15123-1; Q16678; Q05209; P23467; P08575; Q12913; Q15262; Q16827
EC number
EC 2.7.10.1
Uniprot keywords
3D-structure; Alternative splicing; Angiogenesis; ATP-binding; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant; Disulfide bond; EGF-like domain; Glaucoma; Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Proteomics identification; Receptor; Reference proteome; Repeat; Secreted; Signal; Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

34965.9
Length
310
Aromaticity
0.11
Instability index
43.57
Isoelectric point
8.39
Charge

(pH=7)

3.42
2D Binding mode
Binding energy

(Kcal/mol)

-8.67
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
QVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKSRVLSTLSTRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQEDRRER
Hydrogen bonds contact
Hydrophobic contact
57Bifunctional aminoacyl-tRNA synthetase (EPRS)4HVC8.06
Target general information
Gen name
EPRS
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
QPRS; QARS; ProlinetRNA ligase; PIG32; GlutamatylprolyltRNA synthetase; Glutamatyl-prolyl-tRNA synthetase; GluRS; EPRS; Cell proliferationinducing gene 32 protein; Cell proliferation-inducing gene 32
Protein family
Class-I aminoacyl-tRNA synthetase family, Glutamate--tRNA ligase type 2 subfamily; Class-II aminoacyl-tRNA synthetase family
Biochemical class
Carbon-oxygen ligase
Function
The phosphorylation of EPRS, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it to the GAIT complex that binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin), suppressing their translation. Interferon-gamma can therefore redirect, in specific cells, the EPRS function from protein synthesis to translation inhibition. Also functions as an effector of the mTORC1 signaling pathway by promoting, through SLC27A1, the uptake of long-chain fatty acid by adipocytes. Thereby, it also plays a role in fat metabolism and more indirectly influences lifespan. Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA.
Related diseases
Leukodystrophy, hypomyelinating, 15 (HLD15) [MIM:617951]: An autosomal recessive disorder characterized by hypomyelinating leukodystrophy with thinning of the corpus callosum. Clinical features include motor and cognitive impairment appearing in the first or second decade of life, dystonia, ataxia, spasticity, and dysphagia. Most patients develop severe optic atrophy, and some have hearing loss. {ECO:0000269|PubMed:29576217}. The disease may be caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB02684; DB02510; DB03376; DB00142; DB00172
Interacts with
P07814; Q8IWL3; P41252; Q15046; P42695; P54136; O60506
EC number
NA
Uniprot keywords
3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Disease variant; Leukodystrophy; Ligase; Membrane; Metal-binding; Methylation; Multifunctional enzyme; Neurodegeneration; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Proteomics identification; Reference proteome; Repeat; RNA-binding; Translation regulation; Zinc
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

55039.7
Length
483
Aromaticity
0.1
Instability index
39.15
Isoelectric point
5.92
Charge

(pH=7)

-6.4
2D Binding mode
Binding energy

(Kcal/mol)

-9.35
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
GLEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGISEEDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTAMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY
Hydrogen bonds contact
Hydrophobic contact
58Fatty acid-binding protein 5 (FABP5)5UR98.06
Target general information
Gen name
FABP5
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Psoriasis-associated fatty acid-binding protein homolog; PA-FABP; Fatty acid-binding protein, epidermal; Fatty Acid BindingProtein mal1; Epidermal-type fatty acid-binding protein; E-FABP
Protein family
Calycin superfamily, Fatty-acid binding protein (FABP) family
Biochemical class
Fatty acid binding protein
Function
Intracellular carrier for long-chain fatty acids and related active lipids, such as the endocannabinoid, that regulates the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors. Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation. May be involved in keratinocyte differentiation.
Related diseases
Erythrocytosis, familial, 4 (ECYT4) [MIM:611783]: An autosomal dominant disorder characterized by elevated serum hemoglobin and hematocrit, and normal platelet and leukocyte counts. {ECO:0000269|PubMed:18184961, ECO:0000269|PubMed:18378852, ECO:0000269|PubMed:19208626, ECO:0000269|PubMed:22367913}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB03796
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Disulfide bond; Lipid transport; Lipid-binding; Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; Secreted; Synapse; Transport
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

15033.1
Length
134
Aromaticity
0.06
Instability index
28.26
Isoelectric point
6.83
Charge

(pH=7)

-0.14
2D Binding mode
Binding energy

(Kcal/mol)

-8.02
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
ATVQQLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCNFTDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNVTCTRIYEKVE
Hydrogen bonds contact
Hydrophobic contact
59Ecdysone receptor (20-hydroxy-ecdysone receptor) (EcRH) (Ecdysteroid receptor) (Nuclear receptor subfamily 1 group H member 1)3IXP8.05
Target general information
Gen name
NA
Organism
Helicoverpa armigera (Cotton bollworm) (Heliothis armigera)
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
Nuclear hormone receptor family, NR1 subfamily
Biochemical class
NA
Function
NA
Related diseases
NA
Drugs

(DrugBank ID)

NA
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; DNA-binding; Metal-binding; Nucleus; Receptor; Transcription; Transcription regulation; Zinc; Zinc-finger
Protein physicochemical properties
Chain ID
A,D
Molecular weight

(Da)

52799.1
Length
462
Aromaticity
0.09
Instability index
51.97
Isoelectric point
8.09
Charge

(pH=7)

2.37
2D Binding mode
Binding energy

(Kcal/mol)

-9.29
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
QELSIERLLEMESLVADPSEEFQFLRVGPDSNVPPKFRAPVSSLCQIGNKQIAALVVWARDIPHFSQLEMEDQILLIKGSWNELLLFAIAWRSMEFLTSPPQLMCLMPGMTLHRNSALQAGVGQIFDRVLSELSLKMRTLRVDQAEYVALKAIILLNPDVKGLKNRQEVEVLREKMFLCLDEYCRRSRSSEEGRFAALLLRLPALRSISLKSFEHLFFFHLVADTSIAGYIRDALRNHAPPIVPPLTANQKSLIARLVYYQEGYEQMPFRQITEMTILTVQLIVEFAKGLPGFSKISQSDQITLLKACSSEVMMLRVARRYDAATDSVLFANNQAYTRDNYRKAGMAYVIEDLLHFCRCMYSMMMDNVHYALLTAIVIFSDRPGLEQPSLVEEIQRYYLNTLRVYILNQNSASPRSAVIFGKILGILTEIRTLGMQNSNMCISLKLKNRKLPPFLEEIWDVA
Hydrogen bonds contact
Hydrophobic contact
60Melanoma derived growth regulator (MIA)5IXB8.03
Target general information
Gen name
MIA
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Melanoma-derived growth regulatory protein; Melanoma inhibitory activity protein
Protein family
MIA/OTOR family
Biochemical class
NA
Function
Elicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas.
Related diseases
Hypertriglyceridemia, transient infantile (HTGTI) [MIM:614480]: An autosomal recessive disorder characterized by onset of moderate to severe transient hypertriglyceridemia in infancy that normalizes with age. The hypertriglyceridemia is associated with hepatomegaly, moderately elevated transaminases, persistent fatty liver, and the development of hepatic fibrosis. {ECO:0000269|PubMed:22226083, ECO:0000269|PubMed:24549054}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Direct protein sequencing; Disulfide bond; Growth factor; Proteomics identification; Reference proteome; Secreted; SH3 domain; Signal
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

11955.6
Length
105
Aromaticity
0.12
Instability index
26.45
Isoelectric point
8.7
Charge

(pH=7)

2.64
2D Binding mode
Binding energy

(Kcal/mol)

-8.54
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
MPKLADRKLCADQECSHPISMAVALQDYMAPDCRFLTIHRGQVVYVFSKLKGRGRLFWGGSVQGDYYGDLAARLGYFPSSIVREDQTLKPGKVDVKTDKWDFYCQ
Hydrogen bonds contact
Hydrophobic contact